Submit Data |  Help |  Video Tutorials |  News |  Publications |  FTP Download |  REST API |  Citing RGD |  Contact   

Influence of beta,gamma-methyleneadenosine 5'-triphosphate and 2-phosphoglycerate on rat liver phosphoglycerate kinase.

Authors: Lavoinne, A 
Citation: Lavoinne A Biochimie. 1986 Apr;68(4):569-74.
Pubmed: (View Article at PubMed) PMID:3091090

The inhibitory action on rat liver phosphoglycerate kinase of structural analogs of the two substrates of this enzyme (beta,gamma- methyleneadenosine 5'-triphosphate for ATP and 2-phosphoglycerate for 3-phosphoglycerate) was studied. In the direction of ADP utilization, the inhibition patterns obtained with beta,gamma-methyleneadenosine 5'-triphosphate are compatible with the reaction mechanism proposed previously (Lavoinne, A., Marchand, J.C., Chedeville, A. & Matray, F. (1983) Biochimie 65, 211-220). In the direction of ATP utilization, the normally observed nonlinear kinetics were changed into linear kinetics in the presence of these substrate analogs. Our results suggest that saturation of the substrate sites induces a conformational change of the enzyme.

Annotation

Gene Ontology Annotations
Molecular Pathway Annotations
Objects Annotated

Additional Information

 
RGD Object Information
RGD ID: 2302860
Created: 2009-01-19
Species: All species
Last Modified: 2009-01-19
Status: ACTIVE



NHLBI Logo

RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.